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Protein

Acetolactate synthase isozyme 1 small subunit

Gene

ilvN

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

2 pyruvate = 2-acetolactate + CO2.

Pathwayi: L-isoleucine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-isoleucine from 2-oxobutanoate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase isozyme 1 small subunit (ilvN), Acetolactate synthase isozyme 1 large subunit (ilvB), Acetolactate synthase isozyme 2 small subunit (ilvM), Acetolactate synthase isozyme 3 large subunit (ilvI), Acetolactate synthase isozyme 3 small subunit (ilvH), Acetolactate synthase isozyme 2 large subunit (ilvG)
  2. Ketol-acid reductoisomerase (ilvC)
  3. Dihydroxy-acid dehydratase (ilvD)
  4. Branched-chain-amino-acid aminotransferase (ilvE)
This subpathway is part of the pathway L-isoleucine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-isoleucine from 2-oxobutanoate, the pathway L-isoleucine biosynthesis and in Amino-acid biosynthesis.

Pathwayi: L-valine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-valine from pyruvate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase isozyme 1 small subunit (ilvN), Acetolactate synthase isozyme 1 large subunit (ilvB), Acetolactate synthase isozyme 2 small subunit (ilvM), Acetolactate synthase isozyme 3 large subunit (ilvI), Acetolactate synthase isozyme 3 small subunit (ilvH), Acetolactate synthase isozyme 2 large subunit (ilvG)
  2. Ketol-acid reductoisomerase (ilvC)
  3. Dihydroxy-acid dehydratase (ilvD)
  4. Branched-chain-amino-acid aminotransferase (ilvE)
This subpathway is part of the pathway L-valine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-valine from pyruvate, the pathway L-valine biosynthesis and in Amino-acid biosynthesis.

GO - Molecular functioni

  • acetolactate synthase activity Source: EcoCyc
  • amino acid binding Source: InterPro

GO - Biological processi

  • isoleucine biosynthetic process Source: EcoCyc
  • valine biosynthetic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Branched-chain amino acid biosynthesis

Enzyme and pathway databases

BioCyciEcoCyc:SMALLILVN-MONOMER.
ECOL316407:JW3645-MONOMER.
MetaCyc:SMALLILVN-MONOMER.
UniPathwayiUPA00047; UER00055.
UPA00049; UER00059.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetolactate synthase isozyme 1 small subunit (EC:2.2.1.6)
Alternative name(s):
Acetohydroxy-acid synthase I small subunit
Short name:
AHAS-I
Short name:
ALS-I
Gene namesi
Name:ilvN
Ordered Locus Names:b3670, JW3645
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10502. ilvN.

Subcellular locationi

GO - Cellular componenti

  • acetolactate synthase complex Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 9696Acetolactate synthase isozyme 1 small subunitPRO_0000151419Add
BLAST

Proteomic databases

PaxDbiP0ADF8.
PRIDEiP0ADF8.

Interactioni

Subunit structurei

Dimer of large and small chains.

Protein-protein interaction databases

BioGridi4262585. 7 interactions.
IntActiP0ADF8. 6 interactions.
STRINGi511145.b3670.

Structurei

Secondary structure

1
96
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 1610Combined sources
Helixi22 – 3211Combined sources
Beta strandi37 – 448Combined sources
Turni45 – 484Combined sources
Beta strandi49 – 579Combined sources
Helixi62 – 709Combined sources
Beta strandi75 – 817Combined sources
Helixi86 – 949Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LVWNMR-A/B1-96[»]
ProteinModelPortaliP0ADF8.
SMRiP0ADF8. Positions 1-96.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini10 – 8374ACTPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 ACT domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105M71. Bacteria.
COG0440. LUCA.
HOGENOMiHOG000126293.
KOiK01653.
OMAiSHENVIL.
OrthoDBiEOG6X3W8W.
PhylomeDBiP0ADF8.

Family and domain databases

InterProiIPR002912. ACT_dom.
[Graphical view]
PfamiPF01842. ACT. 1 hit.
[Graphical view]
PROSITEiPS51671. ACT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0ADF8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQNTTHDNVI LELTVRNHPG VMTHVCGLFA RRAFNVEGIL CLPIQDSDKS
60 70 80 90
HIWLLVNDDQ RLEQMISQID KLEDVVKVQR NQSDPTMFNK IAVFFQ
Length:96
Mass (Da):11,106
Last modified:December 6, 2005 - v1
Checksum:i7F37DD421EDD3802
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti24 – 241H → D (PubMed:2989782).Curated
Sequence conflicti24 – 241H → D (PubMed:2989781).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02541 Genomic DNA. Translation: CAA26388.1.
L10328 Genomic DNA. Translation: AAA62022.1.
U00096 Genomic DNA. Translation: AAC76693.1.
AP009048 Genomic DNA. Translation: BAE77623.1.
M17102 Genomic DNA. Translation: AAA24719.1.
PIRiG65168. YCEC1S.
RefSeqiNP_418126.1. NC_000913.3.
WP_001181706.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76693; AAC76693; b3670.
BAE77623; BAE77623; BAE77623.
GeneIDi948183.
KEGGiecj:JW3645.
eco:b3670.
PATRICi32122833. VBIEscCol129921_3792.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02541 Genomic DNA. Translation: CAA26388.1.
L10328 Genomic DNA. Translation: AAA62022.1.
U00096 Genomic DNA. Translation: AAC76693.1.
AP009048 Genomic DNA. Translation: BAE77623.1.
M17102 Genomic DNA. Translation: AAA24719.1.
PIRiG65168. YCEC1S.
RefSeqiNP_418126.1. NC_000913.3.
WP_001181706.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LVWNMR-A/B1-96[»]
ProteinModelPortaliP0ADF8.
SMRiP0ADF8. Positions 1-96.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262585. 7 interactions.
IntActiP0ADF8. 6 interactions.
STRINGi511145.b3670.

Proteomic databases

PaxDbiP0ADF8.
PRIDEiP0ADF8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76693; AAC76693; b3670.
BAE77623; BAE77623; BAE77623.
GeneIDi948183.
KEGGiecj:JW3645.
eco:b3670.
PATRICi32122833. VBIEscCol129921_3792.

Organism-specific databases

EchoBASEiEB0497.
EcoGeneiEG10502. ilvN.

Phylogenomic databases

eggNOGiENOG4105M71. Bacteria.
COG0440. LUCA.
HOGENOMiHOG000126293.
KOiK01653.
OMAiSHENVIL.
OrthoDBiEOG6X3W8W.
PhylomeDBiP0ADF8.

Enzyme and pathway databases

UniPathwayiUPA00047; UER00055.
UPA00049; UER00059.
BioCyciEcoCyc:SMALLILVN-MONOMER.
ECOL316407:JW3645-MONOMER.
MetaCyc:SMALLILVN-MONOMER.

Miscellaneous databases

PROiP0ADF8.

Family and domain databases

InterProiIPR002912. ACT_dom.
[Graphical view]
PfamiPF01842. ACT. 1 hit.
[Graphical view]
PROSITEiPS51671. ACT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of the ilvBN operon of Escherichia coli: sequence homologies of the acetohydroxy acid synthase isozymes."
    Wek R.C., Hausser C.A., Hatfield G.W.
    Nucleic Acids Res. 13:3995-4010(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The ilvB locus of Escherichia coli K-12 is an operon encoding both subunits of acetohydroxyacid synthase I."
    Friden P., Donegan J., Mullen J., Tsui P., Freundlich M.
    Nucleic Acids Res. 13:3979-3993(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication."
    Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.
    Genomics 16:551-561(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "Nucleotide sequence of the uhp region of Escherichia coli."
    Friedrich M.J., Kadner R.J.
    J. Bacteriol. 169:3556-3563(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 69-96.
  7. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.

Entry informationi

Entry nameiILVN_ECOLI
AccessioniPrimary (citable) accession number: P0ADF8
Secondary accession number(s): P08143, Q2M7Y3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: December 6, 2005
Last modified: January 20, 2016
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

E.coli contains genes for 3 AHAS isozymes: ilvBN, ilvGM and ilvIH.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.